About Me

My mother was murdered by what I call corporate and political homicide i.e. FOR PROFIT! she died from a rare phenotype of CJD i.e. the Heidenhain Variant of Creutzfeldt Jakob Disease i.e. sporadic, simply meaning from unknown route and source. I have simply been trying to validate her death DOD 12/14/97 with the truth. There is a route, and there is a source. There are many here in the USA. WE must make CJD and all human TSE, of all age groups 'reportable' Nationally and Internationally, with a written CJD questionnaire asking real questions pertaining to route and source of this agent. Friendly fire has the potential to play a huge role in the continued transmission of this agent via the medical, dental, and surgical arena. We must not flounder any longer. ...TSS

aInstitute for Neurodegenerative Diseases, Departments of bNeurology and
cPathology, and dPharmaceutical Chemistry, University of California, San
Francisco, CA 94143 Contributed by Stanley B. Prusiner, May 14, 2014 (sent for
review April 15, 2014)

Abstract Authors & Info SI Metrics PDF PDF + SI Significance
Alzheimer’s disease is the most common neurodegenerative disorder; it is a
progressive dementia for which there is currently no effective therapeutic
intervention. The brains of patients with Alzheimer’s disease exhibit numerous
amyloid β (Aβ) amyloid plaques and tau-laden neurofibrillary tangles. Our
studies show that synthetic Aβ peptides can form prions that infect mice and
induce Aβ amyloid plaque pathology. Two different Aβ prion strains were produced
from Aβ peptides. When injected into transgenic mice, one Aβ strain produced
large plaques and the other strain induced small but more numerous plaques. Our
findings may help to delineate the molecular pathogenesis of Alzheimer’s disease
and the development of anti-Aβ prion therapeutics.

Abstract An increasing number of studies continue to show that the amyloid
β (Aβ) peptide adopts an alternative conformation and acquires transmissibility;
hence, it becomes a prion. Here, we report on the attributes of two strains of
Aβ prions formed from synthetic Aβ peptides composed of either 40 or 42
residues. Modifying the conditions for Aβ polymerization increased both the
protease resistance and prion infectivity compared with an earlier study.
Approximately 150 d after intracerebral inoculation, both synthetic Aβ40 and
Aβ42 prions produced a sustained rise in the bioluminescence imaging signal in
the brains of bigenic Tg(APP23:Gfap-luc) mice, indicative of astrocytic gliosis.
Pathological investigations showed that synthetic Aβ40 prions produced amyloid
plaques containing both Aβ40 and Aβ42 in the brains of inoculated bigenic mice,
whereas synthetic Aβ42 prions stimulated the formation of smaller, more numerous
plaques composed predominantly of Aβ42. Synthetic Aβ40 preparations consisted of
long straight fibrils; in contrast, the Aβ42 fibrils were much shorter. Addition
of 3.47 mM (0.1%) SDS to the polymerization reaction produced Aβ42 fibrils that
were indistinguishable from Aβ40 fibrils produced in the absence or presence of
SDS. Moreover, the Aβ amyloid plaques in the brains of bigenic mice inoculated
with Aβ42 prions prepared in the presence of SDS were similar to those found in
mice that received Aβ40 prions. From these results, we conclude that the
composition of Aβ plaques depends on the conformation of the inoculated Aβ
polymers, and thus, these inocula represent distinct synthetic Aβ prion strains.

Mounting evidence argues that prions feature in the pathogenesis of many,
if not all, neurodegenerative diseases. Such disorders include Alzheimer’s,
Parkinson’s, Lou Gehrig’s and Creutzfeldt-Jakob diseases as well as the
frontotemporal dementias. In each of these illnesses, aberrant forms of a
particular protein accumulate as pathological deposits referred to as amyloid
plaques, neurofibrillary tangles, Lewy bodies, as well as glial cytoplasmic
and/or nuclear inclusions. The heritable forms of the neurodegenerative diseases
are often caused by mutations in the genes encoding the mutant, prion proteins
that accumulate in the CNS of patients with these fatal disorders. The late
onset of the inherited neurodegenerative diseases seems likely to be explained
by the protein quality control systems being less efficient in older neurons and
thus, more permissive for prion accumulation. To date, there is not a single
drug that halts or even slows one neurodegenerative disease.